Header list of 2ez5.pdb file
Complete list - c 21 2 Bytes
HEADER SIGNALLING PROTEIN,LIGASE 10-NOV-05 2EZ5 TITLE SOLUTION STRUCTURE OF THE DNEDD4 WW3* DOMAIN- COMM LPSY PEPTIDE TITLE 2 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE NEDD4; COMPND 3 CHAIN: W; COMPND 4 FRAGMENT: WW3* DOMAIN; COMPND 5 SYNONYM: DNEDD4; COMPND 6 EC: 6.3.2.-; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: COMMISSURELESS LPSY PEPTIDE; COMPND 10 CHAIN: P; COMPND 11 FRAGMENT: RESIDUES 227-237; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER; SOURCE 3 ORGANISM_COMMON: FRUIT FLY; SOURCE 4 ORGANISM_TAXID: 7227; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 MOL_ID: 2; SOURCE 9 SYNTHETIC: YES; SOURCE 10 OTHER_DETAILS: A PEPTIDE COMPRISING RESIDUES 227-237 OF SOURCE 11 COMMISSURELESS FROM DROSOPHILA MELANOGASTER WAS MADE USING STANDARD SOURCE 12 FMOC PEPTIDE SYNTHESIS KEYWDS NEDD4; WW DOMAIN; COMMISSURELESS; PY MOTIF; BINDING AFFINITY, KEYWDS 2 SIGNALLING PROTEIN, LIGASE EXPDTA SOLUTION NMR NUMMDL 30 AUTHOR V.KANELIS,M.C.BRUCE,N.R.SKRYNNIKOV,D.ROTIN,J.D.FORMAN-KAY REVDAT 4 21-DEC-22 2EZ5 1 SEQADV REVDAT 3 09-MAR-22 2EZ5 1 REMARK REVDAT 2 24-FEB-09 2EZ5 1 VERSN REVDAT 1 28-MAR-06 2EZ5 0 JRNL AUTH V.KANELIS,M.C.BRUCE,N.R.SKRYNNIKOV,D.ROTIN,J.D.FORMAN-KAY JRNL TITL STRUCTURAL DETERMINANTS FOR HIGH-AFFINITY BINDING IN A NEDD4 JRNL TITL 2 WW3(*) DOMAIN-COMM PY MOTIF COMPLEX JRNL REF STRUCTURE V. 14 543 2006 JRNL REFN ISSN 0969-2126 JRNL PMID 16531238 JRNL DOI 10.1016/J.STR.2005.11.018 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : ARIA 1.0 REMARK 3 AUTHORS : NILGES, M. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2EZ5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-05. REMARK 100 THE DEPOSITION ID IS D_1000035272. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 288 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 10 MM NA PHOS, 20 MM NACL MM NA REMARK 210 PHOS, 20 MM NACL; 10 MM NA PHOS, REMARK 210 20 MM NACL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1.1 MM DNEDD4 WW3* DOMAIN, U- REMARK 210 13C,U-15N, 1.1 MM COMM LPSY REMARK 210 PEPTIDE, UNLABELLED, 10 MM NA REMARK 210 PHOS, PH 7.0, 20 MM NACL,90% H2O/ REMARK 210 10% D2O; 1.1 MM DNEDD4 WW3* REMARK 210 DOMAIN, U- 13C,U -15N, 1.1 MM REMARK 210 COMM LPSY PEPTIDE, UNLABELLED, REMARK 210 10 MM NA PHOS, PH 7.0, 20 MM REMARK 210 NACL,100% D2O; 1.4 MM DNEDD4 WW3* REMARK 210 DOMAIN, U- 13C,U -15N, 1.0 MM REMARK 210 COMM LPSY PEPTIDE, UNLABELLED, REMARK 210 10 MM NA PHOS, PH 7.0, 20 MM REMARK 210 NACL, 90% H2O/10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 15N; 13C-EDITED NOESY; 3D F1 REMARK 210 -13C; 15N FILTERED NOESY; 2D F1- REMARK 210 13C; 15N F2-13C REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.3, NMRVIEW 5.2.2, ARIA REMARK 210 1.0 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: MIXING TIMES WERE: 175 MS FOR THE 3D F1,F3-13C,15N EDITED REMARK 210 NOESY; 140 FOR THE DOUBLE FILTERED NOESY; 250 FOR THE HALF- REMARK 210 FILTERED NOESY REMARK 215 REMARK 215 NMR STUDY REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON REMARK 215 THESE RECORDS ARE MEANINGLESS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: W, P REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 1 LEU W 523 -71.78 71.81 REMARK 500 1 SER W 525 173.35 62.06 REMARK 500 1 GLU W 527 50.99 -110.84 REMARK 500 1 PRO W 532 179.16 -49.00 REMARK 500 1 ARG W 553 76.44 47.93 REMARK 500 1 ASN W 562 -57.31 -139.26 REMARK 500 1 LEU P 229 76.25 64.01 REMARK 500 1 PRO P 230 99.11 -61.99 REMARK 500 1 SER P 231 156.87 -49.55 REMARK 500 1 TYR P 232 92.16 -50.07 REMARK 500 1 ASP P 233 -32.91 171.51 REMARK 500 1 LEU P 236 35.58 -143.21 REMARK 500 2 LEU W 523 98.72 -66.21 REMARK 500 2 SER W 525 144.89 179.04 REMARK 500 2 GLU W 527 67.26 -150.87 REMARK 500 2 GLU W 529 89.55 61.86 REMARK 500 2 LEU W 531 114.85 59.97 REMARK 500 2 PRO W 532 179.76 -46.50 REMARK 500 2 ARG W 534 73.37 -116.33 REMARK 500 2 SER W 552 20.18 -141.83 REMARK 500 2 ARG W 553 76.17 47.28 REMARK 500 2 ASN W 562 -47.59 -145.28 REMARK 500 2 TYR P 232 86.39 -56.24 REMARK 500 2 ASP P 233 -82.26 177.10 REMARK 500 2 LEU P 236 26.64 -144.03 REMARK 500 3 GLU W 527 47.62 -143.42 REMARK 500 3 GLU W 529 79.34 50.30 REMARK 500 3 PRO W 530 164.55 -47.35 REMARK 500 3 PRO W 532 179.65 -48.15 REMARK 500 3 SER W 552 16.75 -145.90 REMARK 500 3 ASN W 562 -49.36 -144.27 REMARK 500 3 LEU P 229 103.34 -48.25 REMARK 500 3 PRO P 230 -151.63 -58.94 REMARK 500 3 TYR P 232 87.50 -55.40 REMARK 500 3 ASP P 233 -66.29 -177.99 REMARK 500 3 LEU P 236 -45.22 -136.56 REMARK 500 4 LEU W 523 49.08 -158.34 REMARK 500 4 GLU W 528 90.19 69.47 REMARK 500 4 PRO W 532 -178.67 -48.94 REMARK 500 4 SER W 536 -156.31 -146.30 REMARK 500 4 ASN W 562 -48.16 -136.45 REMARK 500 4 TYR P 232 82.19 -60.86 REMARK 500 4 ASP P 233 -50.12 177.17 REMARK 500 5 PRO W 532 -177.66 -48.30 REMARK 500 5 ARG W 553 53.49 74.92 REMARK 500 5 ASN W 562 -67.00 -136.30 REMARK 500 5 ALA W 565 90.61 -57.99 REMARK 500 5 PRO P 230 -172.64 -51.49 REMARK 500 5 ALA P 235 60.26 -156.63 REMARK 500 5 LEU P 236 53.31 -147.76 REMARK 500 REMARK 500 THIS ENTRY HAS 316 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 2EZ5 W 526 566 UNP Q9VVI3 NEDD4_DROME 526 566 DBREF 2EZ5 P 227 237 UNP Q24139 COMM_DROME 227 237 SEQADV 2EZ5 GLY W 521 UNP Q9VVI3 CLONING ARTIFACT SEQADV 2EZ5 PRO W 522 UNP Q9VVI3 CLONING ARTIFACT SEQADV 2EZ5 LEU W 523 UNP Q9VVI3 CLONING ARTIFACT SEQADV 2EZ5 GLY W 524 UNP Q9VVI3 CLONING ARTIFACT SEQADV 2EZ5 SER W 525 UNP Q9VVI3 CLONING ARTIFACT SEQRES 1 W 46 GLY PRO LEU GLY SER GLY GLU GLU GLU PRO LEU PRO PRO SEQRES 2 W 46 ARG TRP SER MET GLN VAL ALA PRO ASN GLY ARG THR PHE SEQRES 3 W 46 PHE ILE ASP HIS ALA SER ARG ARG THR THR TRP ILE ASP SEQRES 4 W 46 PRO ARG ASN GLY ARG ALA SER SEQRES 1 P 11 THR GLY LEU PRO SER TYR ASP GLU ALA LEU HIS SHEET 1 A 3 TRP W 535 VAL W 539 0 SHEET 2 A 3 THR W 545 ASP W 549 -1 O PHE W 546 N GLN W 538 SHEET 3 A 3 ARG W 554 THR W 556 -1 O THR W 556 N PHE W 547 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000 MODEL 1
Complete list - c 21 2 Bytes